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1.
Academic Journal of Second Military Medical University ; (12): 1368-1373, 2012.
Article in Chinese | WPRIM | ID: wpr-839607

ABSTRACT

Glycosylphosphatidylinositol (GPI)-anchored proteins are important cell surface proteins in Candida albicans (C. albicans), and they have important impact on the adhesion, morphogenesis and cell wall synthesis of C. albicans. In recent years, more important functions of GPIanchored proteins have been identified along with the progress in research of C. albicans. By introducing the concept of C. albicans GPIanchored proteins, we reviewed the progress in GPI-anchored proteins research from the perspective of family classification and functional classification, and discussed the future research direction for C. albicans GPI-anchored proteins.

2.
Genet. mol. res. (Online) ; 4(2): 326-345, 30 jun. 2005. tab, ilus
Article in English | LILACS | ID: lil-445284

ABSTRACT

Open reading frames in the transcriptome of Paracoccidioides brasiliensis were screened for potential glycosylphosphatidylinositol (GPI)-anchored proteins, which are a functionally and structurally diverse family of post-translationally modified molecules found in a variety of eukaryotic cells. Numerous studies have demonstrated that various GPI anchor sequences can affect the localization of these proteins in the plasma membrane or the cell wall. The GPI anchor core is produced in the endoplasmic reticulum by sequential addition of monosaccharides and phospho-ethanolamine to phosphatidylinositol. The complete GPI anchor is post-translationally attached to the protein carboxyl-terminus by GPI transamidases. Removal of this GPI lipid moiety by phospholipases generates a soluble form of the protein. The identification of putative GPI-attached proteins in the P. brasiliensis transcriptome was based on the following criteria: the presence of an N-terminal signal peptide for secretion and a hydrophobic region in the C-terminus presenting the GPI-attachment site. The proteins that were identified were in several functional categories: i) eight proteins were predicted to be enzymes (Gel1, Gel2, Gel3, alpha-amylase, aspartic proteinase, Cu-Zn SOD, DFG5, PLB); ii) Ag2/PRA, ELI-Ag1 and Gel1 are probably surface antigens; iii) Crh-like and the GPI-anchored cell wall protein have a putative structural role; iv) ECM33 and Gels (1, 2 and 3) are possibly involved in cell wall biosynthesis, and v) extracellular matrix protein is considered to be an adhesion protein. In addition, eight deduced proteins were predicted to localize in the plasma membrane and six in the cell wall. We also identified proteins involved in the synthesis, attachment and cleaving of the GPI anchor in the P. brasiliensis transcriptome.


Subject(s)
Humans , Open Reading Frames/genetics , Glycosylphosphatidylinositols/analysis , Paracoccidioides/chemistry , Cell Wall/enzymology , Membrane Proteins/genetics , Glycosylphosphatidylinositols/genetics , Paracoccidioides/genetics , Cell Wall/genetics
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